Redox-dependent processes influence most cellular functions, such as differentiation,
proliferation, and apoptosis. Mitochondria are at the center of these processes, as …

Glutaredoxins utilize the reducing power of glutathione to maintain and regulate the cellular
redox state and redox-dependent signaling pathways, for instance, by catalyzing reversible …

Glutaredoxin, Grx, is a small protein containing an active site cysteine pair and was
discovered in 1976 by Arne Holmgren. The Grx system, comprised of Grx, glutathione …

Since their discovery as a substrate for ribonucleotide reductase (RNR), the role of
thioredoxin (Trx) and glutaredoxin (Grx) has been largely extended through their regulatory …

Iron is required to produce haem and iron–sulphur (Fe–S) clusters, processes thought to
occur independently,. Here we show that the hypochromic anaemia in shiraz (sir) zebrafish …

Glutaredoxins (Grxs) are small oxidoreductases that reduce disulphide bonds or protein‐
glutathione mixed disulphides. More than 30 distinct grx genes are expressed in higher …

Glutaredoxins, proteins traditionally involved in redox reactions, are also required for iron–
sulfur cluster assembly and haem biosynthesis. These new roles are probably related to the …

Monothiol glutaredoxins with the CGFS sequence at the active site are widespread among
prokaryotes and eukaryotes. Two subclasses exist, those with a single glutaredoxin domain …

The generation of [4Fe-4S] clusters in mitochondria critically depends, in both yeast and
human cells, on two A-type ISC proteins (in mammals named ISCA1 and ISCA2), which …

Monothiol glutaredoxins play a crucial role in iron–sulfur (Fe/S) protein biogenesis.
Essentially all of them can coordinate a [2Fe-2S] cluster and have been proposed to mediate …